The inhibition of the insulin receptor by the receptor protein PC-1 is not specific and results from the hydrolysis of ATP.
Diabetes
; 45(7): 980-3, 1996 Jul.
Article
en En
| MEDLINE
| ID: mdl-8666152
The membrane protein plasma cell differentiation antigen 1 (PC-1) has been purified as an inhibitor of insulin receptor tyrosine kinase activity and has been implicated in the pathogenesis of NIDDM. However, we show here that PC-1 is a general protein kinase inhibitor in vitro and that this inhibition results from the hydrolysis of ATP by the intrinsic nucleotide pyrophosphatase activity of PC-1. Thus, the inhibition diminished with increasing ATP concentrations, and it was nullified when the ATP concentration was kept constant with a regenerating system or when ATP was added repetitively. When care was taken to avoid ATP depletion, PC-1 did not affect the insulin sensitivity of insulin receptor autophosphorylation. We conclude that the reported inhibition of insulin signaling by PC-1 does not result from a direct inhibition of the insulin receptor kinase activity.
Buscar en Google
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Pirofosfatasas
/
Receptor de Insulina
/
Glicoproteínas de Membrana
/
Adenosina Trifosfato
/
Hidrolasas Diéster Fosfóricas
/
Insulina
Límite:
Animals
/
Female
/
Humans
/
Pregnancy
Idioma:
En
Revista:
Diabetes
Año:
1996
Tipo del documento:
Article
País de afiliación:
Bélgica
Pais de publicación:
Estados Unidos